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Related Experiment Videos

High-activity enzyme-polyurethane coatings.

Géraldine F Drevon1, Karsten Danielmeier, William Federspiel

  • 1Department of Chemical and Petroleum Engineering, University of Pittsburgh, 1249 Benedum Hall, Pennsylvania 15261, USA.

Biotechnology and Bioengineering
|September 5, 2002
PubMed
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This study immobilized diisopropylfluorophosphatase (DFPase) into polyurethane coatings, creating enzyme-containing coatings (ECC) that effectively hydrolyze DFP. Modifying coating hydrophilicity enhanced enzyme activity and stability.

Area of Science:

  • Polymer Chemistry
  • Biocatalysis
  • Materials Science

Background:

  • Enzyme immobilization is crucial for developing reusable biocatalysts.
  • Water-borne polyurethane coatings offer versatile matrices for material functionalization.
  • Diisopropylfluorophosphatase (DFPase) is an enzyme capable of hydrolyzing organophosphates.

Purpose of the Study:

  • To synthesize and characterize enzyme-containing coatings (ECC) by immobilizing DFPase in water-borne polyurethane.
  • To investigate the effect of coating hydrophilicity on DFPase activity and stability within the matrix.
  • To explore the deactivation kinetics of immobilized DFPase.

Main Methods:

  • Synthesis of water-borne polyurethane coatings with co-immobilized diisopropylfluorophosphatase (DFPase).

Related Experiment Videos

  • Characterization of DFPase distribution and activity retention within the coating.
  • Enzymatic hydrolysis assays of diisopropylfluorophosphate (DFP).
  • Modification of coating hydrophilicity by altering polyisocyanate composition.
  • Analysis of DFPase-ECC deactivation kinetics.

    • Main Results:

    • Homogeneous distribution and good activity retention (approx. 39% intrinsic activity) of immobilized DFPase in ECC.
    • Significantly enhanced intrinsic activity of DFPase-ECC when coating hydrophilicity was decreased.
    • Biphasic deactivation kinetics observed, with an initial rapid phase followed by the formation of a hyperstable, active enzyme form.

    Conclusions:

    • Irreversible immobilization of DFPase in polyurethane coatings is feasible, yielding functional ECC.
    • Coating hydrophilicity is a critical parameter for optimizing immobilized enzyme activity.
    • The developed DFPase-ECC exhibits enhanced stability and activity, suggesting potential for applications in organophosphate detoxification.